ID A0A0A1YDY2_9PSED Unreviewed; 448 AA.
AC A0A0A1YDY2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=TMS3_0121565 {ECO:0000313|EMBL:KFX67800.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX67800.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX67800.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX67800.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365093}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU365093}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|RuleBase:RU365093}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX67800.1}.
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DR EMBL; AWSQ01000009; KFX67800.1; -; Genomic_DNA.
DR RefSeq; WP_025167263.1; NZ_AWSQ01000009.1.
DR AlphaFoldDB; A0A0A1YDY2; -.
DR STRING; 1395571.TMS3_0121565; -.
DR eggNOG; COG0845; Bacteria.
DR OrthoDB; 9775513at2; -.
DR Proteomes; UP000030063; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR NCBIfam; TIGR01843; type_I_hlyD; 1.
DR PANTHER; PTHR30386:SF17; ALKALINE PROTEASE SECRETION PROTEIN APRE; 1.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU365093};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU365093}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000030063};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 69..102
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 245..294
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 448 AA; 49312 MW; 5145EF6F98E2DE19 CRC64;
MSDLEFESKS LKLANPAQEV DVDDRRPGRW GMWLVIAGFG GFIIWAVIAP LDAGIVANAT
VNVTDNRKTI QHLTGGSVEA ILVREGDLVK RGQALIELDQ TQAVAEQGVV SAQYIVVRTV
QNRLQAERDG LTEVNFDPDL LARFADDPRL QAAIALQQRL FTTRRNAVIG EAGILQENIR
GAEEQIRGLR QVQGSRRAQI RFLNEELEGV RSLAAEGYVT RNRMLELERS AAELNAALAQ
NIADIGRARN QIAELKLRTL QLEQNFQKEV QSQLTDAQKE ASALTDRLRS LDYEVTHTVI
RSPIDGIVLG LNASTIGGVI QPGSVIMNVV PANEPLQVDA MIPVQAIDKM TPGLPVDITF
PAFNHAQTPS IPGRVLTVSA DRLVDESNKQ PYYLAQVEVT PEGMDKLGSN RIRAGMPATV
TIKTGERNLM SYLMKPMLDR VDNAFKEQ
//
